Vibrational Raman and infrared spectroscopy are used to probe the dynamical, conformational and packing properties associated with lipid-lipid and lipid-protein interactions in membrane assemblies. For example, clathrin, the major structural protein associated with membrane coated pits and cellular coated vesicles, has been implicated in the dynamics of various endocytic processes. Infrared spectrocopy was used to assess the lipid perturbations originating from the interactions of the clathrin coat with the bilayers of the intact, vesicle membranes. Spectra of the about 2850 cm-1 symmetric methylene stretching modes of coated vesicles, uncoated vesicles and synaptic membranes were compared for a wide range of temperatures. Although the bilayer chains are intrinsically dis-ordered because of their heterogeneous composition, further disorder in terms of the introduction of gauche conformers occurs on increasing the temperature of the system. In addition to each membrane system displaying a temperature dependence for the spectroscopic marker reflecting intrachain disorder, the clathrin coated vesicle systems manifest a greater lipid chain disorder, compared to the uncoated vesicles and synaptic membranes, at each temperature studied. This bilayer dis-order induced by the clathrin coat may prove to be one of the major factors responsible for membrane invagination and coated vesicle formation.